Literature DB >> 1616690

Preliminary crystallographic study of peanut peroxidase.

N Ban1, R B van Huystee, J Day, A Greenwood, S Larson, R Esnault, A McPherson.   

Abstract

The cationic isozyme of peroxidase isolated from suspension cultures of peanut cells is a heme-containing and calcium-dependent glycoprotein having four covalently attached oligosaccharide chains. Attempts were made to crystallize the glycoprotein for X-ray diffraction analysis, and these have met with some success. Crystals have now been grown that are suitable for a full three-dimensional structural analysis. The crystals are thin plates and we have shown them to be of the orthorhombic space group P2(1)2(1)2(1) with a = 48.1, b = 97.2, c = 146.2 A. The crystals diffract to beyond 2.8 A resolution, appear to be stable to lengthy X-ray exposure, and contain two molecules of 40,000 daltons each in the asymmetric unit.

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Year:  1992        PMID: 1616690     DOI: 10.1107/s0108768191008807

Source DB:  PubMed          Journal:  Acta Crystallogr B        ISSN: 0108-7681


  1 in total

1.  Analysis of the optical absorption and magnetic-circular-dichroism spectra of peanut peroxidase: electronic structure of a peroxidase with biochemical properties similar to those of horseradish peroxidase.

Authors:  M J Rodríguez Marañón; D Mercier; R B van Huystee; M J Stillman
Journal:  Biochem J       Date:  1994-07-15       Impact factor: 3.857

  1 in total

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